Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea.

Autor: Stefan Schulze, Friedhelm Pfeiffer, Benjamin A Garcia, Mechthild Pohlschroder
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: PLoS Biology, Vol 19, Iss 6, p e3001277 (2021)
Druh dokumentu: article
ISSN: 1544-9173
1545-7885
DOI: 10.1371/journal.pbio.3001277
Popis: Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far. We further show that different N-glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx. volcanii N-glycoproteome revealed here provide new insights into the roles of N-glycosylation in archaeal cell biology.
Databáze: Directory of Open Access Journals
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